Functional role of dimerization of human peptidylarginine deiminase 4 (PAD4). [PDF]
PLoS ONE, 2011 Peptidylarginine deiminase 4 (PAD4) is a homodimeric enzyme that catalyzes Ca²⁺-dependent protein citrullination, which results in the conversion of arginine to citrulline.
Yi-Liang Liu +3 more
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Smoking is not linked to the development of anti-peptidylarginine deiminase 4 autoantibodies in rheumatoid arthritis [PDF]
Arthritis Research & Therapy, 2018 Background Defining environmental factors responsible for development of autoimmunity in rheumatoid arthritis (RA) is critical for understanding mechanisms of disease initiation and propagation. Notably, a history of cigarette smoking has been implicated
Laura C. Cappelli +4 more
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Expression of Peptidylarginine Deiminase Type 4 in Ovarian Tumors [PDF]
International Journal of Biological Sciences, 2010 Peptidylarginine deiminase type 4 (PADI4) converts arginine residues into citrulline. The current study focused on the expression of PADI4 in various subtypes of ovary cancers, and this study investigated the effects of estrogen on PADI4 expression in ...
Lin Wang, Xiaotian Chang, Guangying Yuan, Yan Zhao, Pengcheng Wang
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Anti–Peptidylarginine Deiminase 4 Autoantibodies and Disease Duration as Predictors of Treatment Response in Rheumatoid Arthritis [PDF]
ACR Open RheumatologyBackground Given that autoantibodies to peptidylarginine deiminase 4 (PAD4) are associated with erosive disease in established rheumatoid arthritis (RA), this study was conducted to compare the clinical and prognostic use of anti‐PAD4 antibodies in ...
Laura C. Cappelli +4 more
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Pharmacological targeting of peptidylarginine deiminase 4 prevents cancer-associated kidney injury in mice [PDF]
OncoImmunology, 2017 Renal insufficiency is a frequent cancer-associated problem affecting more than half of all cancer patients at the time of diagnosis. To minimize nephrotoxic effects the dosage of anticancer drugs are reduced in these patients, leading to sub-optimal ...
Jessica Cedervall +8 more
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Probing the Roles of Calcium-Binding Sites during the Folding of Human Peptidylarginine Deiminase 4 [PDF]
Scientific Reports, 2017 Our recent studies of peptidylarginine deiminase 4 (PAD4) demonstrate that its non-catalytic Ca2+-binding sites play a crucial role in the assembly of the correct geometry of the enzyme. Here, we examined the folding mechanism of PAD4 and the role of Ca2+
Yi-Liang Liu +5 more
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Peptidylarginine deiminase 4 -104C/T polymorphism and risk of rheumatoid arthritis: A pooled analysis based on different populations. [PDF]
PLoS ONE, 2018 Many studies have analyzed the association between peptidylarginine deiminase 4 (PADI4) -104C/T polymorphism and rheumatoid arthritis (RA). However, the results are inconsistent. This meta-analysis, based on different populations, updated and reevaluated
Jiong Hua, Weijie Huang
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Frontiers in ImmunologyIntroductionAnti-citrullinated protein antibodies (ACPAs) are a hallmark of rheumatoid arthritis, but the sources of citrullinated antigens as well as which peptidylarginine deiminases (PADs) are required for their production remain incompletely defined.
Caitlyn L Holmes +2 more
exaly +3 more sources
Factors Associated with Promoted Proliferation of Osteosarcoma by Peptidylarginine Deiminase 4. [PDF]
Biomed Res Int, 2021 Osteosarcoma is the most common type of bone malignancy, and the pathogenesis has not been entirely elucidated yet. An important deimination modification enzyme PADI4 (peptidylarginine deiminase 4) has attracted much attention in recent years for its important function in several kinds of human tumors.
Guo J, Yin L, Zhang X, Su P, Zhai Q.
europepmc +4 more sources
Expression of peptidylarginine deiminase 2 and 4 in malignant mesothelioma and its clinical significance [PDF]
Jichu yixue yu linchuang, 2023 Objective To investigate the expression of peptidylarginine deiminase 2 and 4 (PAD2 and PAD4) in malignant mesothelioma (MM), their correlation with citrullinated proteins and clinical significance.
GAN Yihan, SHEN Wei, CHEN Yitong, YAN Kaili, HU Shuaiyue, JIANG Zhaoqiang, YING Shibo
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